Molecular Biology Reports

, Volume 39, Issue 9, pp 9233–9238

Purification and biochemical characterization of a cold-active lipase from Antarctic sea ice bacteria Pseudoalteromonas sp. NJ 70


DOI: 10.1007/s11033-012-1796-4

Cite this article as:
Wang, Q., Hou, Y., Ding, Y. et al. Mol Biol Rep (2012) 39: 9233. doi:10.1007/s11033-012-1796-4


An extracellular cold-active lipase from Antarctic sea ice bacteria Pseudoalteromonas sp. NJ 70 was purified and characterized. The overall purification based on lipase activity was 27.5-fold with a yield of 25.4 %. The purified lipase showed as a single band on SDS-PAGE with an apparent molecular weight of 37 kDa. The optimum temperature and pH were 35 °C and 7.0, respectively. The lipase activity was enhanced by Ca2+ and Mg2+, while was partially inhibited by other metals such as Cu2+, Zn2+, Ba2+, Pb2+, Fe2+ and Mn2+. The lipase had high tolerance to a wide range of NaCl concentrations (0–2 M NaCl). It exhibited high levels of activity in the presence of DTT, Thiourea, H2O2 as well as in the presence of various detergents such as Span 60, Tween-80, Triton X-100. In addition, the lipase showed a preference for long-chain p-nitrophenyl esters (C12–C18). These results indicated that this lipase could be a novel cold-active lipase.


Purification Antarctic Pseudoalteromonas sp. Sea ice Cold-active lipase 

Copyright information

© Springer Science+Business Media B.V. 2012

Authors and Affiliations

  • Quanfu Wang
    • 1
    • 2
  • Yanhua Hou
    • 2
  • Yu Ding
    • 3
  • Peisheng Yan
    • 2
  1. 1.School of Chemical EngineeringHarbin Institute of TechnologyHarbinPeople’s Republic of China
  2. 2.School of Marine and TechnologyHarbin Institute of TechnologyWeihaiPeople’s Republic of China
  3. 3.Fisheries CollegeGuangdong Ocean UniversityZhanjiangPeople’s Republic of China

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